Issue 13, 2006

Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine

Abstract

Controlled protein folding/refolding remains a substantial challenge to the biotechnology industry. Robust and adaptable artificial polymer molecular chaperones could make important contributions towards solving this problem. Taking inspiration from the mechanism of the GroEL/GroES molecular chaperone machine, we report the preparation and testing of a selection of cross-linked thermo-responsive hydrogels, one of which is shown to assist quantitative refolding of a stringent unfolded protein substrate (mitochondrial malate dehydrogenase [mMDH]) during temperature cycling between hydrophobic and hydrophilic states. To our knowledge, this is the first hydrogel-only artificial polymer molecular chaperone to be derived, which is also potentially a generic artificial polymer molecular chaperone for use in a folding bioreactor.

Graphical abstract: Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine

Article information

Article type
Paper
Submitted
15 Mar 2006
Accepted
25 Apr 2006
First published
23 May 2006

Org. Biomol. Chem., 2006,4, 2568-2574

Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine

H. Jones, J. Dalmaris, M. Wright, J. H. G. Steinke and A. D. Miller, Org. Biomol. Chem., 2006, 4, 2568 DOI: 10.1039/B603915D

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